WO1988005818A1 - ADN DE PLASMIDES RECOMBINANT pPR-IL2-19, CODANT POUR LA SYNTHESE D'INTERLEUKINE-2 HUMAINE, PROCEDE POUR SA CONSTRUCTION ET SOUCHE DE BACTERIES ESCHERICHIA COLI VNIIGENETIKA VL 903 (pPR-IL2-19) a TITRE DE PRODUCTEUR D'INTERLEUKINE-2 HUMAINE, LE CONTENANT - Google Patents
ADN DE PLASMIDES RECOMBINANT pPR-IL2-19, CODANT POUR LA SYNTHESE D'INTERLEUKINE-2 HUMAINE, PROCEDE POUR SA CONSTRUCTION ET SOUCHE DE BACTERIES ESCHERICHIA COLI VNIIGENETIKA VL 903 (pPR-IL2-19) a TITRE DE PRODUCTEUR D'INTERLEUKINE-2 HUMAINE, LE CONTENANT Download PDFInfo
- Publication number
- WO1988005818A1 WO1988005818A1 PCT/SU1988/000032 SU8800032W WO8805818A1 WO 1988005818 A1 WO1988005818 A1 WO 1988005818A1 SU 8800032 W SU8800032 W SU 8800032W WO 8805818 A1 WO8805818 A1 WO 8805818A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- plasmid
- gene
- ppr
- human interleukin
- interleukin
- Prior art date
Links
- 239000013612 plasmid Substances 0.000 title claims abstract description 63
- 238000000034 method Methods 0.000 title claims abstract description 14
- 230000015572 biosynthetic process Effects 0.000 title claims abstract description 7
- 238000003786 synthesis reaction Methods 0.000 title claims abstract description 6
- 238000010276 construction Methods 0.000 title abstract description 3
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 title abstract 5
- 102000055277 human IL2 Human genes 0.000 title abstract 5
- 241000588724 Escherichia coli Species 0.000 title abstract 3
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 43
- 239000000203 mixture Substances 0.000 claims abstract description 16
- 102000000588 Interleukin-2 Human genes 0.000 claims abstract description 14
- 108010002350 Interleukin-2 Proteins 0.000 claims abstract description 14
- 239000012634 fragment Substances 0.000 claims abstract description 8
- 229940088710 antibiotic agent Drugs 0.000 claims abstract description 3
- 238000011160 research Methods 0.000 claims abstract description 3
- 238000011835 investigation Methods 0.000 claims description 6
- 230000000977 initiatory effect Effects 0.000 claims description 5
- 238000012360 testing method Methods 0.000 claims description 4
- 241000894006 Bacteria Species 0.000 claims description 2
- 238000010353 genetic engineering Methods 0.000 claims description 2
- 244000005700 microbiome Species 0.000 claims description 2
- 108020004705 Codon Proteins 0.000 claims 2
- 101150072531 10 gene Proteins 0.000 claims 1
- 101150029062 15 gene Proteins 0.000 claims 1
- 108091028043 Nucleic acid sequence Proteins 0.000 claims 1
- 239000011230 binding agent Substances 0.000 claims 1
- 238000002474 experimental method Methods 0.000 claims 1
- 230000001939 inductive effect Effects 0.000 claims 1
- 230000008433 psychological processes and functions Effects 0.000 claims 1
- 239000003242 anti bacterial agent Substances 0.000 abstract description 2
- 239000006152 selective media Substances 0.000 abstract 1
- 230000001131 transforming effect Effects 0.000 abstract 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 20
- 239000000872 buffer Substances 0.000 description 11
- 239000000047 product Substances 0.000 description 8
- 239000007788 liquid Substances 0.000 description 7
- 102000003960 Ligases Human genes 0.000 description 5
- 108090000364 Ligases Proteins 0.000 description 5
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 5
- 229960000723 ampicillin Drugs 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 241000196324 Embryophyta Species 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 239000011541 reaction mixture Substances 0.000 description 4
- 238000009826 distribution Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 238000007363 ring formation reaction Methods 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000007664 blowing Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000008520 organization Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- WSLDOOZREJYCGB-UHFFFAOYSA-N 1,2-Dichloroethane Chemical compound ClCCCl WSLDOOZREJYCGB-UHFFFAOYSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102100022260 Killin Human genes 0.000 description 1
- 101710193777 Killin Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- CTQNGGLPUBDAKN-UHFFFAOYSA-N O-Xylene Chemical compound CC1=CC=CC=C1C CTQNGGLPUBDAKN-UHFFFAOYSA-N 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 244000292604 Salvia columbariae Species 0.000 description 1
- 235000012377 Salvia columbariae var. columbariae Nutrition 0.000 description 1
- 235000001498 Salvia hispanica Nutrition 0.000 description 1
- 241000555745 Sciuridae Species 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O ammonium group Chemical group [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000014167 chia Nutrition 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000002124 endocrine Effects 0.000 description 1
- 210000000744 eyelid Anatomy 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005755 formation reaction Methods 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000009377 nuclear transmutation Methods 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical group 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 230000007096 poisonous effect Effects 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229910052979 sodium sulfide Inorganic materials 0.000 description 1
- GRVFOGOEDUUMBP-UHFFFAOYSA-N sodium sulfide (anhydrous) Chemical compound [Na+].[Na+].[S-2] GRVFOGOEDUUMBP-UHFFFAOYSA-N 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 239000008096 xylene Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/73—Expression systems using phage (lambda) regulatory sequences
Definitions
- Interleukin-2 is an immune modulator of the complex mechanism of action, in particular, it stimulates an immune response due to the activation of comparatively jointly-lymphocytes . , amplification of mitogenesis of stimuli, induction of cytotoxic activity of ⁇ -cells and others.
- the alternative source of interleukin-2 can be used by genetic engineering methods of the microorganism strain, - 2 - carrying regulatory plasmids with the gene of interleukin-2 and ensuring effective expression of this gene.
- the recombinant plasmid Ds which encompass the interleukin-2 human, are known as the recombinant plasmid 5, and the second one is known.
- the means of cooperation are declared recombinant
- 25 plasmid D is included in that, that plasmid ⁇ -23, with a size of 5.4 thousand tons ⁇ . associated with plasmid ⁇ -322 and containing SOS-replica, the gene for the sustainability of acicillin and the second gene of the patient is 2-patient
- SOS modifies by replacing the part of the product for Part I on the site of the distribution in ⁇ II received shimazhu ⁇ 2 ⁇ Z-23 ⁇ is operating;
- the invention is also a strain of the United States Generator 90 903 ( ⁇ - ⁇ 2- ⁇ 9) ⁇ additive producer of an inteleukin-2 people-35 eyelids, which contains a 112-year ⁇ old patient. According to the invention, a method has been obtained. - 6 - for genetic contagion through the introduction of a recumbent plaque ⁇ ⁇ ⁇ ⁇ 2 2- ⁇ 9 ⁇ bacterium ⁇ ⁇ ⁇ ⁇ ⁇ till ⁇ ⁇ .
- the mixture obtained means that the cells are cleaned and that they are inoculated with a medium with an amperage of 15 killin and are secured at a temperature of 28 ° C.
- ⁇ b ⁇ anny ⁇ ⁇ a ⁇ im ⁇ b ⁇ az ⁇ m ⁇ l ⁇ ya ⁇ v vydelyayu ⁇ ⁇ lazmidnuyu D ⁇ ⁇ b ⁇ znachennuyu ⁇ a ⁇ ⁇ - ⁇ 2- ⁇ 9, in ⁇ y ⁇ chn ⁇ s ⁇ v ⁇ ss ⁇ edineniya ⁇ ashen ⁇ v ⁇ ve ⁇ yayu ⁇ v ⁇ ss ⁇ an ⁇ vle- 20 Niemi on s ⁇ y ⁇ e is ⁇ dny ⁇ uchas ⁇ v D ⁇ ⁇ anee ⁇ su ⁇ s ⁇ vuyuschey ⁇ sled ⁇ va ⁇ eln ⁇ s ⁇ i recognition ⁇ es ⁇ i ⁇ azy ⁇ z ⁇ .
- the claimed sh ⁇ amm ⁇ .s ⁇ ⁇ IIgene ⁇ i ⁇ a ⁇ 903 ( ⁇ - ⁇ 2- ⁇ luchayu ⁇ ⁇ ans ⁇ matsiey ⁇ etsi ⁇ ien ⁇ n ⁇ g ⁇ sh ⁇ amma ba ⁇ e ⁇ y ⁇ zs ⁇ eg ⁇ s ⁇ a s ⁇ ⁇ e ⁇ mbinan ⁇ n ⁇ y ⁇ lazmidn ⁇ y D ⁇ 25 ⁇ - ⁇ 2- ⁇ 9 ..
- the Storm of E. genetics ⁇ 903 ( ⁇ - ⁇ 2- ⁇ 9) is characterized by the following symptoms.
- the battery is damaged by a simple and liquid synthetic, semi-synthetic, and complex environment.
- the boulevard When growing on an aggre- gated boulevard in Hortingburg, the boulevard will develop smooth, round, weak 20 worn out mild formations.
- When cultivated in a liquid it is a type of bouillon or ⁇ 9 with an open-ended mixture, and a similar suspension is obtained.
- the batteries are suitable for a range of temperatures from 5 to 40 ° C (optimum 37 ° C) 25 to 6.7-7.5.
- carbohydrates for example, sugar
- amino acids are used as a source of carbon.
- nitrogen can serve as mineral salts in the ammonium form, as well as organic compounds in the form of a substance, a substance, a burned 30 amine.
- the strain is susceptible to amperage at a concentration of up to 100 mg / l and cultivated in liquids and on aggre-ated nutritional products.
- 3 mcg of plasmid ⁇ 40 promotes the release of 1 ⁇ 1 ⁇ in 60 ⁇ l of buffer for restorative- ⁇ containing
- DBD is disposed of for volume of this alcohol.
- the plant is 10 msec ⁇ 2 0.
- the processing plant is 30 msec in size, and contains 30 msec.
- Plasma plasmid ⁇ institutions24 expands the products and the other type of Bacillus in 70 ⁇ l of buffer for Test- ⁇ , containing 10 ⁇ pis- ⁇ , ⁇ 7.9, 6 m ⁇ 2 , 6
- the efficiency of the transmutation makes up 5 * 10 per I ig of the native plasmid ⁇ 24 • Stops obliques that are stable to ampicillin (100 g / ml), from below
- plasmid ⁇ 2 ⁇ -23 ⁇ is produced.
- the plasmid ⁇ 2 ⁇ -3 with a size of 5.4 thousand n.p., is based on the basic plasmid ⁇ -322 and
- the linearized plasmid ⁇ 24 ⁇ is combined with the plasmid fragment ⁇ 2 ⁇ -23 ⁇ .
- I mcg plasmid J and 2 mcg fragment process the J-ligase phage ⁇ 4 in the bushe for 15 ligations and the volume of the reaction mixture is 30 ⁇ l.
- the plasmid J is isolated, as described above, and advances the direct analysis.
- the cultural density of the seed crop is 1.5–2.5 units.
- the product is equipped with a control system equipped with a temperature regulating system
- 35 for optical density equal to 3.5 at 550 nm, at a temperature of 28 ° C, and then carry out the thermal induction, increasing - 15 - a temperature of 42-45 ° C for 5 minutes, after which they continue for another 2 hours.
- a synthetic human protein was received from the integrated cell protein from the I ml of the commercial liquid, and the catering is supplied.
- the product analyzes the elec- trophoresis in a 15% polylamide gel in the presence of a 0.1% sodium sulfide solution. Proteins separated in le are parsed in the factory of the Humassi 250-250 Zegrá / ⁇ standard method. The white content of whites in the area is divided after scanning on the densitel gel.
- the zone of interleukin appears in the form of a brown cover for an unfulfilled window of a non-filtering cell.
- the synthesized protein products of the gene for interleukin-2 it makes up to $ 12 of the total amount of the battery in the cell. Intended use
- the inventive recombinant plasmid J ⁇ - ⁇ 2- ⁇ - 16 - cadreuyu synthesis of interleukin-2 people find an application for receiving strains-beneficiaries of interleukin-2 people with high activity.
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- Toxicology (AREA)
- Virology (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Priority Applications (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP88502088A JPH01502639A (ja) | 1987-02-09 | 1988-02-08 | ヒトインターロイキン―２の合成についてコードする組換えプラスミドＤＮＡｐＰＲ―１Ｌ２―１９、その工学的作出方法及びそれを含有するヒトインターロイキン―２産生細菌大腸菌ＶＮ２ジェネティカＶＬ９０３（ｐＰＲ―１Ｌ２―１９）株 |
| NL8820102A NL8820102A (nl) | 1987-02-09 | 1988-02-08 | Recombinant plasmide-dna ppr-il2-19 dat de synthese van menselijk interleukine-2 codeert, werkwijze voor de bereiding daarvan en bacteriestam escherichia coli vniigenetika vl 903 (ppr-il2-19) die menselijk interleukine-2 produceert en het plasmide-dna bevat. |
| HU881691A HUT50873A (en) | 1987-02-09 | 1988-02-08 | Process for producing recombinant plasmid dna encoding human interleukin-2 and escherichia coli comprising same |
| DE883890052T DE3890052T1 (de) | 1987-02-09 | 1988-02-08 | Rekombination-plasmid-dns ppr-il2-i9, die die synthese des menschlichen interleukin-2 kodiert, verfahren zu ihrem konstruieren und stamm der bakterien escherichia coli vniigenetika vl 903 (ppr-il2-i9)-produzent des menschlichen interleukin-2, der dieselbe enthaelt |
| FI884557A FI884557A7 (fi) | 1987-02-09 | 1988-10-04 | Rekombinantplasmid-dna ppr-il2-19, som kodas foer syntes av maenniskans interleukin-2, foerfarande foer framstaellning daerav och stammen bacteria escherichia coli vniigenetika vl 903 (ppr-19) producerande maenniskans interleukin-2 och innehaollande detta dna. |
| GB8823729A GB2210373A (en) | 1987-02-09 | 1988-10-10 | Recombinant plasmid dna ppr-il2-19,coding for synthsis of human interleukin-2 and strain of bacteria escherichia coli vniigenetika vl 903 (ppr-il2-19) |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SU874191353A SU1703693A1 (ru) | 1987-02-09 | 1987-02-09 | Рекомбинантна плазмидна ДНК @ - @ 2-19, кодирующа синтез интерлейкина-2 человека, способ ее конструировани @ штамм бактерий ЕSснеRIснIа coLI - продуцент интерлейкина-2 человека |
| SU4191353/28 | 1987-02-09 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1988005818A1 true WO1988005818A1 (fr) | 1988-08-11 |
Family
ID=21284358
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/SU1988/000032 WO1988005818A1 (fr) | 1987-02-09 | 1988-02-08 | ADN DE PLASMIDES RECOMBINANT pPR-IL2-19, CODANT POUR LA SYNTHESE D'INTERLEUKINE-2 HUMAINE, PROCEDE POUR SA CONSTRUCTION ET SOUCHE DE BACTERIES ESCHERICHIA COLI VNIIGENETIKA VL 903 (pPR-IL2-19) a TITRE DE PRODUCTEUR D'INTERLEUKINE-2 HUMAINE, LE CONTENANT |
Country Status (10)
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6068993A (en) * | 1997-07-02 | 2000-05-30 | Biobras Sa | Vector for expression of heterologous protein and methods for extracting recombinant protein and for purifying isolated recombinant insulin |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0088195A2 (en) * | 1981-12-28 | 1983-09-14 | Takeda Chemical Industries, Ltd. | Messenger RNA, production and use thereof |
| EP0194818A2 (en) * | 1985-03-11 | 1986-09-17 | Takeda Chemical Industries, Ltd. | Production of interleukin-2 |
| WO1986006410A1 (en) * | 1985-04-30 | 1986-11-06 | Takeda Chemical Industries, Ltd. | Process for increasing yield of interleukin-2 |
-
1987
- 1987-02-09 SU SU874191353A patent/SU1703693A1/ru active
-
1988
- 1988-02-08 JP JP88502088A patent/JPH01502639A/ja active Pending
- 1988-02-08 HU HU881691A patent/HUT50873A/hu unknown
- 1988-02-08 DE DE883890052T patent/DE3890052T1/de not_active Withdrawn
- 1988-02-08 NL NL8820102A patent/NL8820102A/nl not_active Application Discontinuation
- 1988-02-08 CH CH3816/88A patent/CH676997A5/de not_active IP Right Cessation
- 1988-02-08 WO PCT/SU1988/000032 patent/WO1988005818A1/ru active Application Filing
- 1988-10-04 FI FI884557A patent/FI884557A7/fi not_active Application Discontinuation
- 1988-10-07 SE SE8803566A patent/SE8803566D0/xx not_active Application Discontinuation
- 1988-10-10 GB GB8823729A patent/GB2210373A/en not_active Withdrawn
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0088195A2 (en) * | 1981-12-28 | 1983-09-14 | Takeda Chemical Industries, Ltd. | Messenger RNA, production and use thereof |
| EP0194818A2 (en) * | 1985-03-11 | 1986-09-17 | Takeda Chemical Industries, Ltd. | Production of interleukin-2 |
| WO1986006410A1 (en) * | 1985-04-30 | 1986-11-06 | Takeda Chemical Industries, Ltd. | Process for increasing yield of interleukin-2 |
Also Published As
| Publication number | Publication date |
|---|---|
| DE3890052T1 (de) | 1989-04-13 |
| SE8803566L (sv) | 1988-10-07 |
| NL8820102A (nl) | 1989-01-02 |
| GB8823729D0 (en) | 1988-12-07 |
| FI884557A0 (fi) | 1988-10-04 |
| CH676997A5 (enrdf_load_stackoverflow) | 1991-03-28 |
| SU1703693A1 (ru) | 1992-01-07 |
| HUT50873A (en) | 1990-03-28 |
| FI884557A7 (fi) | 1988-10-04 |
| JPH01502639A (ja) | 1989-09-14 |
| SE8803566D0 (sv) | 1988-10-07 |
| GB2210373A (en) | 1989-06-07 |
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